MolNFT v1 · #122128 · protein

Crystal structure of S. rosetta camkii kinase domain

5IG1 · CAMK/CAMK2 protein kinase: “Crystal structure of S. rosetta camkii kinase domain”. X-ray diffraction, 1 ligand (PO4), 6 pockets (best druggability 0.72). MolNFT v1 #122128 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5IG1
Type: protein
Length: 604 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAMK/CAMK2 protein kinase
UniProt: F2UPG5
Ligands: PO4
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CAMK/CAMK2 protein kinase	protein	300	41% helix, 17% strand	F2UPG5
B	CAMK/CAMK2 protein kinase	protein	304	36% helix, 16% strand	F2UPG5

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	709	0.72	0.79	71	empty
2	451	0.66	0.78	35	empty
3	104	0.58	0.85	21	empty
4	194	0.52	0.78	32	empty
5	117	0.49	0.79	18	empty

Interfaces

1 interface between chains.

A–B · 739 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5IG1 · Crystal structure of S. rosetta CaMKII kinase domain · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F2UPG5
Elsewhere: RCSB PDB 5IG1 · PDBe 5IG1 · UniProt F2UPG5

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